SHORTENED CECROPIN-A MELITTIN HYBRIDS - SIGNIFICANT SIZE-REDUCTION RETAINS POTENT ANTIBIOTIC-ACTIVITY
SHORTENED CECROPIN-A MELITTIN HYBRIDS - SIGNIFICANT SIZE-REDUCTION RETAINS POTENT ANTIBIOTIC-ACTIVITY
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DOI：
10.1016/0014-5793(92)80377-s
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发表时间：
1992-01-20
期刊：
影响因子：
3.5
通讯作者：
BOMAN, HG
中科院分区：
文献类型：
--
作者：
ANDREU, D;UBACH, J;BOMAN, HG
我们之前报道了由天蚕素A（CA）和蜂毒肽（M）的不同片段组成的两种26残基抗菌肽。我们现在报告，高活性杂合体 CA(1-8)M(1-18) 的 C 端部分尺寸大幅减小，产生了一系列 20、18 和 15 残基类似物，其抗生素特性与较大分子相似。特别是，15个残基杂合体CA(1-7)M(2-9)、CA(1-7)M(4-11)和CA(1-7)M(5-12)是迄今为止描述的最短的基于天蚕素的肽抗生素，其抗菌活性和谱与天蚕素A相似或更好，并且尺寸减小了60%。它们的尺寸减小和高度α螺旋结构需要一种替代机制来与细菌膜相互作用。
We have earlier reported two 26-residue antibacterial peptides made up from different segments of cecropin A (CA) and melittin (M). We now report a substantial reduction in size at the C-terminal section of the highly active hybrid CA(1-8)M(1-18), leading to a series of 20-, 18- and 15-residue analogs with antibiotic properties similar to the larger molecule. In particular, the 15-residue hybrids CA(1-7)M(2-9), CA(1-7)M(4-11) and CA(1-7)M(5-12) are the shortest cecropin-based peptide antibiotics described so far, with antibacterial activity and spectra similar or better than cecropin A and a 60% reduction in size. Their reduced size and highly alpha-helical structure require an alternative mechanism for their interaction with bacterial membranes.